CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001048
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heme oxygenase 2 
Protein Synonyms/Alias
 HO-2 
Gene Name
 Hmox2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
198VDNAQQFKQFYRARMubiquitination[1]
213NALDLNLKTKERIVEubiquitination[1]
258GLPVHDGKGDIRKCPubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. 
Sequence Annotation
 REPEAT 263 268 HRM 1.
 REPEAT 280 285 HRM 2.
 METAL 44 44 Iron (heme axial ligand) (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Oxidoreductase; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 315 AA 
Protein Sequence
MSSEVETSEG VDESEKNSMA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN 60
IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKAALIK DMKYFFGENW 120
EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG 180
EGTQFYLFEH VDNAQQFKQF YRARMNALDL NLKTKERIVE EANKAFEYNM QIFSELDQAG 240
SMLARETLED GLPVHDGKGD IRKCPFYAAQ PDKGTLGGSN CPFQTTVAVL RKPSLQLILA 300
ASVALVAGLL AWYYM 315 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006788; P:heme oxidation; IEA:InterPro.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IEA:Compara. 
Interpro
 IPR002051; Haem_Oase.
 IPR016053; Haem_Oase-like.
 IPR016084; Haem_Oase-like_multi-hlx.
 IPR018207; Haem_oxygenase_CS. 
Pfam
 PF01126; Heme_oxygenase 
SMART
  
PROSITE
 PS00593; HEME_OXYGENASE 
PRINTS
 PR00088; HAEMOXYGNASE.